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J Biol Chem, Vol. 273, Issue 44, 29272-29277, October 30, 1998
2-Glycoprotein I Macrophage Interactions
From the Department of Cell Biology, The University of Texas
M. D. Anderson Cancer Center, Houston, Texas 77030
The binding and uptake of phosphatidylserine
(PS)-expressing cells appears to involve multiple receptor-mediated
systems that recognize the lipid either directly or indirectly through
intermediate proteins that form a molecular bridge between the cells.
Here we show that 
2-glycoprotein I
(2GPI), a 50-kDa serum glycoprotein, binds PS-containing
vesicles and serves as an intermediate for the interaction of these
vesicles with macrophages. Chemical modification of lysines and
cysteines abolished 2GPI-dependent PS uptake
by inhibiting the binding of PS to 2GPI and the binding
of PS·2GPI complex to macrophages, respectively.
Recognition was mediated by 2GPI and not by the lipid
because antibodies to 2GPI inhibited binding of the
complex to macrophages. These results indicate that human
(THP-1-derived) macrophages bind 2GPI only after it is
bound to its lipid ligand. Competition experiments with monosaccharides that inhibit lectin-dependent interactions, and
PS·2GPI binding experiments using deglycosylated
2GPI, suggested that carbohydrate residues were not
required for macrophage recognition of the complex. Antibodies to
putative macrophage PS receptors (CD36, CD68, and CD14) did not inhibit
uptake of the complex. These data suggest that 2GPI can
bind cells that fail to maintain membrane lipid asymmetry and generate
a specific bridging moiety that is recognized for clearance by a
phagocyte receptor that is distinct from CD36, CD68, and CD14.
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